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Q27772

- C1TC_SPOFR

UniProt

Q27772 - C1TC_SPOFR

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Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene
N/A
Organism
Spodoptera frugiperda (Fall armyworm)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 1723NADPBy similarity
Nucleotide bindingi378 – 3858ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: UniProtKB-EC
  3. methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB-EC
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB-EC

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. histidine biosynthetic process Source: UniProtKB-KW
  3. methionine biosynthetic process Source: UniProtKB-KW
  4. purine nucleotide biosynthetic process Source: UniProtKB-KW
  5. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
OrganismiSpodoptera frugiperda (Fall armyworm)
Taxonomic identifieri7108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeAmphipyrinaeSpodoptera

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000199325Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ27772.
SMRiQ27772. Positions 10-294, 467-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 303303Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
BLAST
Regioni51 – 555Substrate bindingBy similarity
Regioni98 – 1003Substrate bindingBy similarity
Regioni270 – 2745Substrate bindingBy similarity
Regioni304 – 933630Formyltetrahydrofolate synthetaseAdd
BLAST

Domaini

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27772-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV
60 70 80 90 100
YIRMKLRAAE NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM
110 120 130 140 150
PLDSVHPIDS HAITDAVSPD KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC
160 170 180 190 200
VELIKRTGVT IAGKNVVVLG RSRIVGTPVS ELLKWEHATV TVCHSKTKNL
210 220 230 240 250
SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS DPTKKSGQRL
260 270 280 290 300
VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT
310 320 330 340 350
WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK
360 370 380 390 400
AKISLSVLDR MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG
410 420 430 440 450
RNSFAVMRQP SQGPTFGVKG GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA
460 470 480 490 500
NNLLAAQMDA RIFHELTQKD GPLFDRLVPK IKGVRKFSPI QLRRLKRLGI
510 520 530 540 550
TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR KITVGQSPTE
560 570 580 590 600
KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA
610 620 630 640 650
DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD
660 670 680 690 700
KIAMKLAGEN GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR
710 720 730 740 750
ALKMHGGGPP VSAGMPLNDV YVQENLELLS KGLCNLGKHI SNGNKFGVPV
760 770 780 790 800
VVAINKHGND TPAELNLVKE FAVKNGAFRA VLCDHWAKGG LGALELADAV
810 820 830 840 850
IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT DEVLEKIKTF
860 870 880 890 900
TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP
910 920 930
MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF
Length:933
Mass (Da):100,618
Last modified:January 16, 2004 - v3
Checksum:i55C3FA820C1A55CB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36189 mRNA. Translation: AAA74302.1.
PIRiS53523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36189 mRNA. Translation: AAA74302.1 .
PIRi S53523.

3D structure databases

ProteinModelPortali Q27772.
SMRi Q27772. Positions 10-294, 467-528.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00193 .

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda."
    Tremblay G.B., MacKenzie R.E.
    Biochim. Biophys. Acta 1261:129-133(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiC1TC_SPOFR
AccessioniPrimary (citable) accession number: Q27772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: October 29, 2014
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3